| General Information |
| MoonProt ID | 135 |
| First appeared in release | 1.0 |
| Name(s) | Ketol-acid reductoisomerase
Acetohydroxy-acid reductoisomerase
Alpha-keto-beta-hydroxylacyl reductoisomerase
Gene Name: ILV5
|
| UniProt ID | P06168 (ILV5_YEAST), Reviewed |
| GO terms | GO:0000002 mitochondrial genome maintenance
GO:0008652 cellular amino acid biosynthetic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009097 isoleucine biosynthetic process
GO:0009099 valine biosynthetic process
GO:0055114 oxidation-reduction process
GO:0003690 double-stranded DNA binding
GO:0004455 ketol-acid reductoisomerase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0050662 coenzyme binding
GO:0005739 mitochondrion
GO:0042645 mitochondrial nucleoid |
| Organisms for which functions have been demonstrated | Saccharomyces cerevisiae (yeast, fungi) |
| Sequence length | 394 |
| FASTA sequence | >gi|609403|gb|AAB67753.1| Ilv5p: acetohydroxyacid reductoisomerase [Saccharomyces cerevisiae]
MLRTQAARLICNSRVITAKRTFALATRAAAYSRPAARFVKPMITTRGLKQINFGGTVETVYERADWPREKLLDYFKNDTFALIGYGSQGYGQGLNLRDNGLNVIIGVRKDGASWKAAIEDGWVPGKNLFTVEDAIKRGSYVMNLLSDAAQSETWPAIKPLLTKGKTLYFSHGFSPVFKDLTHVEPPKDLDVILVAPKGSGRTVRSLFKEGRGINSSYAVWNDVTGKAHEKAQALAVAIGSGYVYQTTFEREVNSDLYGERGCLMGGIHGMFLAQYDVLRENGHSPSEAFNETVEEATQSLYPLIGKYGMDYMYDACSTTARRGALDWYPIFKNALKPVFQDLYESTKNGTETKRSLEFNSQPDYREKLEKELDTIRNMEIWKVGKEVRKLRPENQ
|
| Structure Information |
| PDB ID | 1NP3 3FR8 1YRL |
| Quaternary structure | |
| SCOP | NAD(P)-binding Rossmann-fold domains, phosphogluconate dehydrogenase C-terminal domain-like, |
| CATH | 3.40.50.720, 6.10.240.10 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-36, 367-373, 391-395 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | acetohydroxyacid reductoisomerase, enzyme
Amino-acid biosynthesis, L-leucine, L-isoleucine and L-valine biosynthesis
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+ => (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ => (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH
Cofactor
|
| References for function | JM Baterman, PS Perlman, and RA Butow. (2002) Mutational Bisection of the Mitochondrial DNA Stability and Amino Acid Biosynthetic Functions of Ilv5p of Budding Yeast. Genetics. 161, 1043-1052.
PMID: 12136009 |
| E.C. number | 1.1.1.86 |
| Location of functional site(s) | |
| Cellular location of function | mitochondrion |
| Comments | NADPH Binding: Glu319, His226, Glu311, Asp315, Lys252, Glu492, Glu496, Ser518.
R Dumas, V Biou, F Halgand, et al. (2001) Enzymology, Structure, and Dynamics of Acetohydroxy Acid Isomeroreductase. Accou. Of Chem. Res. 34, 399-408.
Mg Binding: Asp315, Glu319. NADPH Binding: Gly132, Gly134, Glu136, Glu143, Asp146, Val258, Val259, Gly265, Arg162, Ser165, Ser167.
F Halgand, E Dumas, V Biou, et al. (1999) Characterization of the Conformational Changes of Acetohydroxy Acid Isomeroreductase Induced by the Binding of Mg 2+ Ions, NADPH, and a Competitive Inhibitor. Biochemistry. 38, 6025-6034.
Mn and ADP binding: Asp315, Glu496, Ser518.
K Thomazeau, R Dumas, F Halgand, et al. (2000) Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose. Acta. Cryst. 56, 389-397. |
| Function 2 |
| Function description | maintain mitochondrial DNA stability
enzyme catalytic function not needed for this role |
| References for function | O Zelenaya-Troitskaya, PS Perlman, and RA Butow. (1995) An enzyme in yeast mitochondria that catalyzes a step in branched-chain amino acid biosynthesis also functions in mitochondria DNA stability. The EMBO Journ. 14, 3268-3276.
PMID: 7621838.
JM Baterman, PS Perlman, and RA Butow. (2002) Mutational Bisection of the Mitochondrial DNA Stability and Amino Acid Biosynthetic Functions of Ilv5p of Budding Yeast. Genetics. 161, 1043-1052.
PMID: 12136009. |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | mitochondria |
| Comments | |